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P08515

- GST26_SCHJA

UniProt

P08515 - GST26_SCHJA

Protein

Glutathione S-transferase class-mu 26 kDa isozyme

Gene
N/A
Organism
Schistosoma japonicum (Blood fluke)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
    GST isoenzymes appear to play a central role in the parasite detoxification system. Other functions are also suspected including a role in increasing the solubility of haematin in the parasite gut.

    Catalytic activityi

    RX + glutathione = HX + R-S-glutathione.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei111 – 1111SubstrateCurated

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase class-mu 26 kDa isozyme (EC:2.5.1.18)
    Short name:
    GST 26
    Alternative name(s):
    Sj26 antigen
    SjGST
    OrganismiSchistosoma japonicum (Blood fluke)
    Taxonomic identifieri6182 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaPlatyhelminthesTrematodaDigeneaStrigeididaSchistosomatoideaSchistosomatidaeSchistosoma

    Pathology & Biotechi

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 218217Glutathione S-transferase class-mu 26 kDa isozymePRO_0000185805Add
    BLAST

    Proteomic databases

    PRIDEiP08515.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi6182.P08515.

    Structurei

    Secondary structure

    1
    218
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 118
    Helixi12 – 143
    Helixi15 – 2410
    Beta strandi29 – 335
    Helixi35 – 373
    Helixi38 – 447
    Turni45 – 473
    Beta strandi55 – 595
    Beta strandi64 – 674
    Helixi68 – 7811
    Helixi86 – 11025
    Helixi115 – 13622
    Turni137 – 1393
    Beta strandi145 – 1473
    Helixi150 – 16516
    Turni167 – 1726
    Helixi174 – 18512
    Helixi187 – 1937
    Beta strandi195 – 1973
    Beta strandi203 – 2075
    Beta strandi209 – 2113
    Beta strandi213 – 2153

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1B8XX-ray2.70A2-218[»]
    1BG5X-ray2.60A1-218[»]
    1DUGX-ray1.80A/B2-218[»]
    1GNEX-ray2.50A2-218[»]
    1GTAX-ray2.40A1-218[»]
    1GTBX-ray2.60A1-218[»]
    1M99X-ray2.30A1-218[»]
    1M9AX-ray2.10A1-218[»]
    1M9BX-ray2.60A1-218[»]
    1U87X-ray3.50A1-218[»]
    1U88X-ray3.50A/B1-218[»]
    1UA5X-ray2.50A1-218[»]
    1Y6EX-ray3.00A/B2-218[»]
    3CRTX-ray1.90A1-214[»]
    3CRUX-ray2.30A1-214[»]
    3D0ZX-ray2.50A1-214[»]
    3QMZX-ray6.00S/T2-218[»]
    4AI6X-ray3.40A/B2-218[»]
    4AKGX-ray3.30A/B2-218[»]
    4AKHX-ray3.60A/B2-218[»]
    4AKIX-ray3.70A/B2-218[»]
    4ECBX-ray2.20A/B1-218[»]
    4ECCX-ray2.20A1-215[»]
    ProteinModelPortaliP08515.
    SMRiP08515. Positions 2-218.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08515.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8382GST N-terminalAdd
    BLAST
    Domaini85 – 203119GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni7 – 82Glutathione binding
    Regioni41 – 455Glutathione binding
    Regioni54 – 552Glutathione binding
    Regioni67 – 682Glutathione binding

    Sequence similaritiesi

    Belongs to the GST superfamily. Mu family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiNOG300089.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P08515-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL    50
    EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL 100
    DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH 150
    PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA 200
    WPLQGWQATF GGGDHPPK 218
    Length:218
    Mass (Da):25,499
    Last modified:January 23, 2007 - v3
    Checksum:i5E2AC418BD0EF13F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14654 mRNA. Translation: AAB59203.1.
    PIRiA61514.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M14654 mRNA. Translation: AAB59203.1 .
    PIRi A61514.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1B8X X-ray 2.70 A 2-218 [» ]
    1BG5 X-ray 2.60 A 1-218 [» ]
    1DUG X-ray 1.80 A/B 2-218 [» ]
    1GNE X-ray 2.50 A 2-218 [» ]
    1GTA X-ray 2.40 A 1-218 [» ]
    1GTB X-ray 2.60 A 1-218 [» ]
    1M99 X-ray 2.30 A 1-218 [» ]
    1M9A X-ray 2.10 A 1-218 [» ]
    1M9B X-ray 2.60 A 1-218 [» ]
    1U87 X-ray 3.50 A 1-218 [» ]
    1U88 X-ray 3.50 A/B 1-218 [» ]
    1UA5 X-ray 2.50 A 1-218 [» ]
    1Y6E X-ray 3.00 A/B 2-218 [» ]
    3CRT X-ray 1.90 A 1-214 [» ]
    3CRU X-ray 2.30 A 1-214 [» ]
    3D0Z X-ray 2.50 A 1-214 [» ]
    3QMZ X-ray 6.00 S/T 2-218 [» ]
    4AI6 X-ray 3.40 A/B 2-218 [» ]
    4AKG X-ray 3.30 A/B 2-218 [» ]
    4AKH X-ray 3.60 A/B 2-218 [» ]
    4AKI X-ray 3.70 A/B 2-218 [» ]
    4ECB X-ray 2.20 A/B 1-218 [» ]
    4ECC X-ray 2.20 A 1-215 [» ]
    ProteinModelPortali P08515.
    SMRi P08515. Positions 2-218.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 6182.P08515.

    Chemistry

    DrugBanki DB00143. Glutathione.
    DB01058. Praziquantel.

    Proteomic databases

    PRIDEi P08515.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG300089.

    Miscellaneous databases

    EvolutionaryTracei P08515.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mr 26,000 antigen of Schistosoma japonicum recognized by resistant WEHI 129/J mice is a parasite glutathione S-transferase."
      Smith D.B., Davern K.M., Board P.G., Tiu W.U., Garcia E.G., Mitchell G.F.
      Proc. Natl. Acad. Sci. U.S.A. 83:8703-8707(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Smith D.B., Davern K.M., Board P.G., Tiu W.U., Garcia E.G., Mitchell G.F.
      Proc. Natl. Acad. Sci. U.S.A. 84:6541-6541(1987)
      Cited for: SEQUENCE REVISION.
    3. "Expression of an enzymatically active parasite molecule in Escherichia coli: Schistosoma japonicum glutathione S-transferase."
      Smith D.B., Rubira M.R., Simpson R.J., Davern K.M., Tiu W.U., Board P.G., Mitchell G.F.
      Mol. Biochem. Parasitol. 27:249-256(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-15.
    4. "Three-dimensional structure of Schistosoma japonicum glutathione S-transferase fused with a six-amino acid conserved neutralizing epitope of gp41 from HIV."
      Lim K., Ho J.X., Keeling K., Gilliland G.L., Ji X., Ruker F., Carter D.C.
      Protein Sci. 3:2233-2244(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
    5. "Crystal structures of a schistosomal drug and vaccine target: glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel."
      McTigue M.A., Williams D.R., Tainer J.A.
      J. Mol. Biol. 246:21-27(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH INHIBITOR PRAZIQUANTEL.
    6. "Characterization of the electrophile binding site and substrate binding mode of the 26-kDa glutathione S-transferase from Schistosoma japonicum."
      Cardoso R.M., Daniels D.S., Bruns C.M., Tainer J.A.
      Proteins 51:137-146(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH GLUTATHIONE ANALOGS.
    7. "Using affinity chromatography to engineer and characterize pH-dependent protein switches."
      Sagermann M., Chapleau R.R., DeLorimier E., Lei M.
      Protein Sci. 18:217-228(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-214.

    Entry informationi

    Entry nameiGST26_SCHJA
    AccessioniPrimary (citable) accession number: P08515
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 105 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    Miscellaneous

    There are at least two isoenzymes of GST in S.japonicum.

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3